-transparent.png){kind=logo}
Inhibitors of protein synthesis capable of differential effects on nascent peptide synthesis on membrane-bound and free polyribosomes were employed to investigate the structure and function of cellular membranes of liver. The formation of membranous whorls in the cytoplasm and distension of nuclear membranes were induced by inhibitors of protein synthesis (i.e., cycloheximide and emetine) which predominantly interfere with nascent peptide synthesis on membrane-bound polyribosomes in situ. Other inhibitors of protein synthesis such as puromycin and fusidic acid, which inhibit nascent peptide synthesis on both free and membrane-bound polyribosomes, and chloramphenicol, which inhibits mitochondrial protein synthesis, did not induce these alterations. Cycloheximide, puromycin, and chloramphenicol produce some common cellular lesions as reflected by similar alterations in morphology, such as swelling of mitochondria, degranulation of rough endoplasmic reticulum, and aggregation of free ribosomes. The process of whorl formation in the cytoplasm, the incorporation of [(3)H]leucine and of [(3)H]choline into endoplasmic reticulum and the total NADPH-cytochrome c reductase activity of the endoplasmic reticulum were determined. During maximum formation of membranous whorls, [(3)H]leucine incorporation into cytoplasmic membranes was inhibited, while [(3)H]choline incorporation into these structures was increased; maximum inhibition of protein synthesis and stimulation of choline incorporation into endoplasmic reticulum, however, preceded whorl formation. Cycloheximide decreased the activity of NADPH-cytochrome c reductase of rough endoplasmic reticulum, but increased NADPH-cytochrome c reductase activity of smooth endoplasmic reticulum. In addition, cycloheximide decreased the content of hemoprotein in both the microsomal and mitochondrial fractions of rat liver, and the activities of mixed function oxidase and of oxidative phosphorylation were impaired to different degrees. Succinate-stimulated microsomal oxidation was also inhibited. The possible mechanisms involved in the formation of membranous whorls, as well as their functions, are discussed.
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
January 1967,
The Journal of biological chemistry,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
April 1981,
Experientia,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
January 1976,
Progress in liver diseases,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
June 1984,
Molecular and cellular biochemistry,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
May 1969,
The Journal of cell biology,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
June 1975,
FEBS letters,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
December 1982,
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
September 1972,
Experientia,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
July 1981,
Biochimica et biophysica acta,
K M Hwang, and
L C Yang, and
C K Carrico, and
R A Schulz, and
J B Schenkman, and
A C Sartorelli
November 1967,
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
